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박수영,서희원,왕남웅,김대회,여인환,최동호,Park. Soo Young,Seo. Hee Won,Wang. Nam Woong,Kim. Dae Hoi,Yeo. In Hwan,Choi. Dong Ho 한국방재학회 2014 한국방재학회논문집 Vol.14 No.2
국외에서는 용도 및 창의 크기를 제한하여 방화구획에 비차열 방화유리의 사용을 허용하는데 반해 국내에는 그 사용이 불가능하다. 따라서, 국내의 비차열 방화유리의 내화성능을 확인하고, 화재안전성을 평가해 볼 필요성이 있다. 본 연구에서는 비차열 방화유리에 대하여 면적별로 4가지 실험체를 구성하여 내화실험을 실시하고, 측정된 복사열유량 및 온도를 적용하여 화재안전성을 평가하였다. 그 결과 화재안전성을 확보하면서 사용이 가능한 면적비를 제안하였다. In foreign countries, a non-insulated fire glazed window is permitted in fire compartment restricting the use and size, but on the domestic side, not permitted. So, there is a need to confirm the fire resistance of the domestic non-insulated fire glazed window and to evaluate the fire safety of that. In this study, the fire resistance tests of 4 types of windows were conducted depending on window area, and the measured radiant heat fluxes and temperatures were evaluated in fire safety. As a result, we suggested the window/wall area ratio secured the fire safety.
당뇨유발쥐에서 닭의장풀의 혈당감소효과와 간조직내의 Glucose-6-Phosphate Dehydrogenase의 효소활성에 미치는 효과
박수영,조경혜,Park, Soo-Young,Cho, Kyung-Hea 한국생약학회 1994 생약학회지 Vol.25 No.3
The hypoglycemic and metabolic effects of Commelina communis L. extract were investigated in alloxan induced diabetic rats. The increased blood glucose level in the diabetic rats was significantly reduced and the loss of body weight was recovered with the treatment of the plant protein fractions($30{\sim}70%$ ammonium sulfate precipitates). Administration of the plant protein fractions elicited the significant increase of glucose-6-phosphate dehydrogenase (G-6-P DH) activity and liver weight which were decreased in the diabetic rat liver. G-6-P DH was partially purified from extract- or insulin-treated diabetics, diabetic control, and normal rat liver and studied for the biochemical properties. The $K_m$ value(9.002 mM) of diabetic rat liver enzyme was greatly higher than that (0.033 mM) of normal enzyme indicating the affinity of enzyme for the substrate was significantly reduced in the diabetic rat liver. This reduced affinity of enzyme for the substrate in the diabetic rat was recovered in the extract- or insulin-treated rat liver enzyme having 0.164 or 0.208 mM of their $K_m$ values, respectively. Although there was no significant difference in the optimum pH(6.0) and optimum temperature($37^{\circ}C$) of enzyme among the experimental groups, the dependence of their activities on pH appeared to be slightly resistant in the extract- or insulin-treated group compared to the diabetic group. In order to investigate the antigenicity of rat liver enzyme among experimental groups, enzyme-linked immunosorbent assay was carried out by using anti-G-6-P DH anti-serum. Absorbance(0.102) shown in the normal rat liver was reduced even below zero in the alloxan-diabetic rat liver, but increased again in the extract- or insulin-treated rat liver(0.096 or 0.118, respectively). The result of this study suggested that G-6-P DH may be used as a marker enzyme to diagnose and to indicate the progress of the diabetics, and the hypoglycemic effect of the extracts of Commelina communis L. was certainly associated with action or mode of G-6-P DH on the rat liver.
Kluyverromyces fragilis의 Alkaline Phosphatase 유전자의 구조 분석
박수영,황선갑,하상철,김종국,박완,홍순덕,Park, Soo-Young,Hwang, Seon-Gap,Ha, Sang-Chul,Kim, Jong-Guk,Park, Wan,Hong, Soon-Duck 한국미생물·생명공학회 1994 한국미생물·생명공학회지 Vol.22 No.1
From the pSKH201 plasmid which had been previously cloned in our laboratory, a 3.0kbp insert DNA encoding the alkaline phosphatase of Kluyveromyces fragilis was cleaved with several restriction endonucleases and ligated int the appropriate sites of M13mp18/19 vectors and sequenced by Sanger's dideoxy chain termination method. The sequence contained a 1,638 bp open reading frame(ORP) whose similarities in nucleotide, when compared with those of Saccharomyces cerevisiae and Escherichia coli by GENETYX program, were found to be 61% and 46%, respectively. The deduced amino acid sequence consists of 546 amino acids and contains several homologous regions in the alkaline phosphatases of E. coli, S.cerevisiae and human placenta.
Espression of Alkaline Phosphatase Gene from Kluyveromyces fragilis in E. coli and S. cerevisiae
박수영,황선갑,이동선,김종국,남주현,홍순덕,Park, Soo-Young,Hwang, Seon-Kap,Lee, Dong-Sun,Kim, Jong-Guk,Nam, Joo-Hyun,Hong, Soon-Duck 한국미생물 · 생명공학회 1995 한국미생물·생명공학회지 Vol.23 No.2
The alkaline phosphatase (K-ALPase) gene of Kluyveromyces fragilis has been cloned (1) and determined its base sequences (2) previously in our laboratory. When the K-ALPase gene was expressed in Escherichia coli and Saccharomyces cerevisiae, it showed a constitutive activity in E. coli, and a derepressed activity in S. cerevisiae in phosphate-limited medium. Northem hybridization experiment was performed to elucidate the transcription level of the K-ALPase gene. Northern experiment showed that transcription level of K-ALPase gene in S. cerevisiae was higher in phosphate depletion, but it was higher in high phosphate medium than in phosphate limited medium in K. fragilis. The transcription initiation site of the K-ALPase gene was determined by primer extension analysis. It matched nucleotide position - 169 in relation to the putative trnslational start site.
고구마 배양세포에서 Peroxiredoxin cDNA의 분리 및 발현 특성
박수영,류선화,권석윤,김종국,곽상수,Park, Soo-Young,Ryu, Sun-Hwa,Kwon, Suk-Yoon,Kim, Jong-Guk,Kwak, Sang-Soo 한국식물생명공학회 2003 식물생명공학회지 Vol.30 No.2
Peroxiredoxin(Pix) are large family of peroxidases that reduce alkyl hydroperoxides and hydrogen peroxide. A cDNA clone (referred to as swPrxl) encoding Pix was from a sweetpotato cDNA library constructed from suspension-sultured cells, and its expression was investigated in terms of stress. The swPrxl contained an open reading frame (ORF) encoding mature protein of 193 amino acids with calculated molecular mass of 20.8kDa. The predicted amino acid sequence of swPrxl has two conserved cysteines that are essential resicues for the reduction of peroxides. It showed high amino acid sequence homology ot PixIIF of Arabidopsis (77%) and putative Prx of rice(72%). RNA gel-blot analysis showed that swPrxl gene was expressed dominantly in leave among intact tissues, and also highly detect in suspension-cultured cells. Interestingly, the level of swPrxl transcripts was almost the same regardless of the growth stage in suspension culture. Furthermore, the transcription level of swPrxl gene was not significantly changed in response to various stress treatments such as wounding, extreme temperature and stress-related chemicals RT-PCR analyses.